Improving the emulsifying properties of whey protein isolate-citrus pectin blends by a novel reactive extrusion approach

被引：17

作者：

Koch, L. ^{[1
]}

Hummel, L. ^{[1
]}

Schuchmann, H. P. ^{[1
]}

Emin, M. A. ^{[1
]}

机构：

[1] Karlsruhe Inst Technol, Inst Proc Engn Life Sci Food Proc Engn, Karlsruhe, Germany

来源：

JOURNAL OF FOOD ENGINEERING | 2018年 / 223卷

关键词：

Reactive extrusion; Whey protein; Citrus pectin; Emulsion; Maillard reaction; Covalent cross-links; MAILLARD REACTION; RHEOLOGICAL PROPERTIES; ELEVATED-TEMPERATURES; FUNCTIONAL-PROPERTIES; BETA-LACTOGLOBULIN; STATE DIAGRAM; SOY PROTEIN; SLIT DIE; DENATURATION; TRANSGLUTAMINASE;

D O I：

10.1016/j.jfoodeng.2017.10.027

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

In this study we used a new experimental setup to improve the emulsifying capacity of whey protein isolate-citrus pectin (WPI-HMCP) blends during extrusion processing. In this setup, the extruder serves as pump, while the reaction takes place mainly in a 380 mm long slit die which is attached at the end of the extruder. Using this setup, it is possible to improve the emulsifying capacity of WPI-HMCP blends: The Sauter mean diameter of emulsions stabilized by the extruded blends could be reduced compared to those stabilized by the untreated blend. The smallest Sauter mean diameter was measured when the WPI-HMCP blend was treated at 120 degrees C for 46 s residence time in the reaction die (corresponding to a total mass flow rate of 19.4 kg/h). It was halved compared to the untreated blend. Structural analyses of the reaction products showed that at constant reaction die temperature and increasing total mass flow rate the formation of disulfide bonds is favored, while the formation of non-disulfide covalent cross-links is inhibited. (C) 2017 Elsevier Ltd. All rights reserved.

引用

页码：175 / 188

页数：14

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